Article
Covalent binding of flavins to RnfG and RnfD in the Rnf complex from Vibrio cholerae.
Biochemistry - 28 Oct 2008
Backiel Julianne, Juárez Oscar, Zagorevski Dmitri V, Wang Zhenyu, Nilges Mark J, Barquera Blanca
Abstract excerpt
Enzymes of the Rnf family are believed to be bacterial redox-driven ion pumps, coupling an oxidoreduction process to the translocation of Na+ across the cell membrane. Here we show for the first time that Rnf is a flavoprotein, with FMN covalently bound to threonine-175 in RnfG and a second flavin bound to threonine-187 in RnfD. Rnf subunits D and G are homologous to subunits B and C of Na+-NQR, respectively....
Topics
- Amino Acid Motifs
- Amino Acid Sequence
- Bacterial Proteins
- Cholera
- Flavin Mononucleotide
- Flavin-Adenine Dinucleotide
- Flavins
- Flavoproteins
- Genes, Bacterial
- Models, Biological
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction
- Quinone Reductases
